ID CYSH_SODGM Reviewed; 244 AA. AC Q2NVN2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Phosphoadenosine phosphosulfate reductase; DE EC=1.8.4.8; DE AltName: Full=PAPS reductase, thioredoxin dependent; DE AltName: Full=PAdoPS reductase; DE AltName: Full=3'-phosphoadenylylsulfate reductase; DE AltName: Full=PAPS sulfotransferase; GN Name=cysH; OrderedLocusNames=SG0518; OS Sodalis glossinidius (strain morsitans). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Sodalis. OX NCBI_TaxID=343509; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16365377; DOI=10.1101/gr.4106106; RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., RA Hattori M., Aksoy S.; RT "Massive genome erosion and functional adaptations provide insights RT into the symbiotic lifestyle of Sodalis glossinidius in the tsetse RT host."; RL Genome Res. 16:149-156(2006). CC -!- FUNCTION: Reduction of activated sulfate into sulfite. CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + sulfite + CC thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 3/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP008232; BAE73793.1; -; Genomic_DNA. DR RefSeq; YP_454198.1; -. DR SMR; Q2NVN2; 2-230. DR GeneID; 3868219; -. DR GenomeReviews; AP008232_GR; SG0518. DR KEGG; sgl:SG0518; -. DR NMPDR; fig|343509.6.peg.1173; -. DR HOGENOM; Q2NVN2; -. DR OMA; Q2NVN2; TRFNGLK. DR BioCyc; SGLO343509:SG0518-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredo...; IEA:HAMAP. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfa...; IEA:HAMAP. DR HAMAP; MF_00063; -; 1. DR InterPro; IPR004511; PAdo_PSO4_Rdtase_CysH. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR011800; PAPS_reductase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Pfam; PF01507; PAPS_reduct; 1. DR TIGRFAMs; TIGR00434; cysH; 1. DR TIGRFAMs; TIGR02057; PAPS_reductase; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Oxidoreductase. FT CHAIN 1 244 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_1000008940. SQ SEQUENCE 244 AA; 27701 MW; 6D744EBCB80A3900 CRC64; MSDWDLGELN ALEKAQQTAA LAAVNQQLES QTAEQRVAWA LEHLPEQAVL SSSFGIQAAV SLRLVTRQRP DIPVILTDTG YLFPETYRFI DELTETLGLN LQIFRATTSP AWQEARYGKL WEQGVEGIER YNQLNKVEPM NRALATLGAG TWFAGLRREQ SGSRAHLPVL AIQRGVFKLL PIIDWDNRQV YQYLTRHGLS YHPLWEQGYL SVGDTHTTRK CEPGMSEEET RFFGLKRECG LHEG //